ID D2WK08_HETGA Unreviewed; 328 AA.
AC D2WK08;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Rhodopsin {ECO:0000256|ARBA:ARBA00013487, ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
GN Name=RHO {ECO:0000313|EMBL:ADB45246.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:ADB45246.1};
RN [1] {ECO:0000313|EMBL:ADB45246.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20016835; DOI=10.1371/journal.pone.0008326;
RA Zhao H., Ru B., Teeling E.C., Faulkes C.G., Zhang S., Rossiter S.J.;
RT "Rhodopsin molecular evolution in mammals inhabiting low light
RT environments.";
RL PLoS ONE 4:E8326-E8326(2009).
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000256|ARBA:ARBA00004504}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU004951}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000256|PIRSR:PIRSR600732-50}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000256|RuleBase:RU004951}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ290307; ADB45246.1; -; Genomic_DNA.
DR AlphaFoldDB; D2WK08; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProt.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd15080; 7tmA_MWS_opsin; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR PANTHER; PTHR24240; OPSIN; 1.
DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRSR:PIRSR600732-
KW 50};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600732-3};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU004951};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600732-
KW 4}; Lipoprotein {ECO:0000256|PIRSR:PIRSR600732-5};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|RuleBase:RU004951};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951};
KW Retinal protein {ECO:0000256|ARBA:ARBA00022925,
KW ECO:0000256|PIRSR:PIRSR600732-50};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|RuleBase:RU004951};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004951};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004951};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW Zinc {ECO:0000256|PIRSR:PIRSR600732-1}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 244..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 273..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 44..296
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT SITE 103
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT MOD_RES 286
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT LIPID 312
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-5"
FT LIPID 313
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-5"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4"
FT DISULFID 100..177
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADB45246.1"
FT NON_TER 328
FT /evidence="ECO:0000313|EMBL:ADB45246.1"
SQ SEQUENCE 328 AA; 36874 MW; 96516E3F9CB9504B CRC64;
VPFSNITGMV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPVNFLTLY VTVQHKKLRT
PLNYILLNLA VADLFMVICG FTTTLYTSMH GYFVFGATGC NMEGFFATLG GEIALWSLVV
LAIERYMVVC KPMSNFRFGE NHAIVGVAFT WVMALACAAP PLAGWSRYIP EGMQCSCGID
YYTPKPEINN ESFVIYMFVV HFTIPLVIIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
TRMVIIMVIA FLICWVPYAS VAMYIFTHQG SDFGPIFMTI PAFFAKSSSI YNPVIYIMMN
KQFRNCMLTT ICCGKSPLGD DEASTTAS
//
